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Comparative Study
. 1997 Sep 19;90(6):1085-95.
doi: 10.1016/s0092-8674(00)80374-8.

Cloning and crystal structure of hematopoietic prostaglandin D synthase

Y Kanaoka  1 , H Ago, E Inagaki, T Nanayama, M Miyano, R Kikuno, Y Fujii, N Eguchi, H Toh, Y Urade, O Hayaishi
Affiliations
Free article
Comparative Study

Cloning and crystal structure of hematopoietic prostaglandin D synthase

Y Kanaoka et al. Cell. .
Free article

Erratum in

  • Cell 1999 Feb 5;96(3):449

Abstract

Hematopoietic prostaglandin (PG) D synthase is the key enzyme for production of the D and J series of prostanoids in the immune system and mast cells. We isolated a cDNA for the rat enzyme, crystallized the recombinant enzyme, and determined the three-dimensional structure of the enzyme complexed with glutathione at 2.3 A resolution. The enzyme is the first member of the sigma class glutathione S-transferase (GST) from vertebrates and possesses a prominent cleft as the active site, which is never seen among other members of the GST family. The unique 3-D architecture of the cleft leads to the putative substrate binding mode and its catalytic mechanism, responsible for the specific isomerization from PGH2 to PGD2.

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